Evidence map›Paper›PMID 41629458›Full record

ArticleScientific reports2026

Orbitrap Astral-based proteome and phosphoproteome analysis identifies candidate proteins associated with the phosphatidate phosphatase MoPah1 in Magnaporthe oryzae.

Juan Zhao, Lili Yang, Xinyi Shi, Xinmei Zou, Bo Liu, Yong Wu, Chengming Zhang, Lan Xiang

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Article in Scientific reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

8 authors.

Juan ZhaoCollege of Chemistry and Life Sciences, Sichuan Provincial Key Laboratory for Development and Utilization of Characteristic Horticultural Biological Resources, Chengdu Normal University, Chengdu, 611130, China. zhaojuan201809@163.com.
Lili YangNovogene Corporation Incorporated Company, Beijing, 100000, China.
Xinyi ShiCollege of Chemistry and Life Sciences, Sichuan Provincial Key Laboratory for Development and Utilization of Characteristic Horticultural Biological Resources, Chengdu Normal University, Chengdu, 611130, China.
Xinmei ZouCollege of Chemistry and Life Sciences, Sichuan Provincial Key Laboratory for Development and Utilization of Characteristic Horticultural Biological Resources, Chengdu Normal University, Chengdu, 611130, China.
Bo LiuCollege of Chemistry and Life Sciences, Sichuan Provincial Key Laboratory for Development and Utilization of Characteristic Horticultural Biological Resources, Chengdu Normal University, Chengdu, 611130, China.
Yong WuCollege of Chemistry and Life Sciences, Sichuan Provincial Key Laboratory for Development and Utilization of Characteristic Horticultural Biological Resources, Chengdu Normal University, Chengdu, 611130, China.
Chengming ZhangCollege of Chemistry and Life Sciences, Sichuan Provincial Key Laboratory for Development and Utilization of Characteristic Horticultural Biological Resources, Chengdu Normal University, Chengdu, 611130, China.
Lan XiangCollege of Chemistry and Life Sciences, Sichuan Provincial Key Laboratory for Development and Utilization of Characteristic Horticultural Biological Resources, Chengdu Normal University, Chengdu, 611130, China.

Funding

National Natural Science Foundation of China 32402340Natural Science Foundation of Sichuan, China 2024NSFSC1320
6 · The paper itself

Abstract

backgroundPrevious studies have shown that the phosphatidate phosphatase MoPah1 plays a critical role in Magnaporthe oryzae development and pathogenicity. The gene deletion mutant exhibits reduced virulence on rice leaves; however, the MoPah1 regulatory network remains unclear.

resultIn this study, we applied a quantitative data-independent acquisition approach using the Orbitrap Astral instrument to analyze the gene deletion mutant. We identified 6,799 proteins and 15,682 phosphorylation sites in M. oryzae, with differentially abundant proteins primarily enriched in metabolic and autophagy pathways. Integrating phosphoproteomic and proteomic analyses, we found 72 overlapping proteins. Additionally, we employed glutathione S-transferase pull-down and yeast two-hybrid assays to screen and verify MoPah1-interacting proteins, identifying Pmk1.

conclusionsOur findings reveal candidate proteins in the MoPah1 regulatory network and the interaction between MoPah1 and Pmk1 in M. oryzae.

Indexed as

Fungal ProteinsMagnaporthePhosphatidate PhosphatasePhosphoproteinsProteomeProteomicsAscomycotaOryzaPhosphorylationFungal ProteinsPhosphatidate PhosphatasePhosphoproteinsProteomeMagnaporthe oryzaePhosphatidate phosphatasePhosphoproteomicsProteomic

Identifiers

PMID41629458
PMCPMC12917106

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